蛋白質立体構造の安定性
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概要
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Three-dimensional structures of proteins determined by X-ray crystallography provide important clues on the molecular mechanism of protein folding, which is the last step of gene expression. The present status on the native structures revealed from the accumulated data is reviewed. Furthermore, the stability of a native conformation is dependent on the environment of a protein molecule such as temperature, and denaturation from a native state occurs as the transition of two states, the native and denatured states. The denaturation phenomenon is analyzed in terms of intermolecular interactions. The understanding of the protein architecture may be essential for the progress of the protein engineering.
- 日本結晶学会の論文